Dear Crystallographers (teleology-haters exempt here),
Does anyone know of any references discussing teleology of inverted repeats in transporters, i.e., what design sense does it make to use this architecture, why is it so common even in the absence of sequence similarity? Is there some underlying feature of this general design principle that helps transporters work well? I suspect someone has discussed it somewhere?
Similarly, generally, with regard to oligomers, which are so common: what's the advantage? Isn't it just as likely to generate a protein-protein interface of proteins AB as making an AA interface? Or perhaps it's not? It just seems to me that oligomerization is way too over-represented in the structural world to be by chance.
All the best,
Jacob
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Jacob Pearson Keller, PhD
Looger Lab/HHMI Janelia Farms Research Campus
19700 Helix Dr, Ashburn, VA 20147
email: [log in to unmask]
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